ArticlePloS one2013
Tenascin C promiscuously binds growth factors via its fifth fibronectin type III-like domain.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers, 1 of them a synthesis that pooled it.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
66 citing papers in PubMed, 1 synthesis or guideline pooled it, 125 citations in OpenAlex.
- Does Tenascin have Clinical Implications in Pathological Grade of Glioma Patients?: A Systematic Meta-Analysis.Medicine · 2015Pooled it
- Bone Extracellular Matrix-Inspired Biomaterials for Enhanced Bone Repair.International journal of nanomedicine · 2026Review
- The Role of Tenascin-C in Neuroinflammation and Neuroplasticity.International journal of molecular sciences · 2025Review
- Deciphering the Tenascin-C Nexus: A Comprehensive Review of Its Involvement in Chronic Respiratory Diseases.Pathophysiology : the official journal of the International Society for Pathophysiology · 2025Review
- Tenascin-C promotes bone regeneration via inflammatory macrophages.Cell death and differentiation · 2025Article
- Cisplatin resistance alters ovarian cancer spheroid formation and impacts peritoneal invasion.Frontiers in cell and developmental biology · 2025Article
- The role of TNC in atherosclerosis and drug development opportunities.International journal of biological sciences · 2024Review
- Matricellular Proteins in the Homeostasis, Regeneration, and Aging of Skin.International journal of molecular sciences · 2023Review
- Tenascin-C in Tissue Repair after Myocardial Infarction in Humans.International journal of molecular sciences · 2023Article
- Investigating Chemokine-Matrix Networks in Breast Cancer: Tenascin-C Sets the Tone for CCL2.International journal of molecular sciences · 2023Article
- How the mechanobiology orchestrates the iterative and reciprocal ECM-cell cross-talk that drives microtissue growth.Science advances · 2023Article
- Framing Heartaches: The Cardiac ECM and the Effects of Age.International journal of molecular sciences · 2023Review
- Extracellular matrix composition affects outgrowth of dendrites and dendritic spines on cortical neurons.Frontiers in cellular neuroscience · 2023Article
- A virological view of tenascin-C in infection.American journal of physiology. Cell physiology · 2023Review
- Matrix protein Tenascin-C promotes kidney fibrosis via STAT3 activation in response to tubular injury.Cell death & disease · 2022Article
- Bioactive extracellular matrix fragments in tendon repair.Cell and tissue research · 2022Review
- Advances on the roles of tenascin-C in cancer.Journal of cell science · 2022Article
- The fibrogenic niche in kidney fibrosis: components and mechanisms.Nature reviews. Nephrology · 2022Review
- Tenascin-C in fibrosis in multiple organs: Translational implications.Seminars in cell & developmental biology · 2022Review
- Focus on the Contribution of Oxidative Stress in Skin Aging.Antioxidants (Basel, Switzerland) · 2022Review
6 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tenascin C (TNC) is an extracellular matrix protein that is upregulated during development as well as tissue remodeling. TNC is comprised of multiple independent folding domains, including 15 fibronectin type III-like (TNCIII) domains. The fifth TNCIII domain (TNCIII5) has previously been shown to bind heparin. Our group has shown that the heparin-binding fibronectin type III domains of fibronectin (FNIII), specifically FNIII12-14, possess affinity towards a large number of growth factors. Here, we show that TNCIII5 binds growth factors promiscuously and with high affinity. We produced recombinant fragments of TNC representing the first five TNCIII repeats (TNCIII1-5), as well as subdomains, including TNCIII5, to study interactions with various growth factors. Multiple growth factors of the platelet-derived growth factor (PDGF) family, the fibroblast growth factor (FGF) family, the transforming growth factor beta (TGF-β) superfamily, the insulin-like growth factor binding proteins (IGF-BPs), and neurotrophins were found to bind with high affinity to this region of TNC, specifically to TNCIII5. Surface plasmon resonance was performed to analyze the kinetics of binding of TNCIII1-5 with TGF-β1, PDGF-BB, NT-3, and FGF-2. The promiscuous yet high affinity of TNC for a wide array of growth factors, mediated mainly by TNCIII5, may play a role in multiple physiological and pathological processes involving TNC.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.